RapamycinFungusV1, Main, Exploration, bibRecord, 000D50

Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2.

Identifieur interne : 000D50 ( Main/Exploration ); précédent : 000D49; suivant : 000D51

Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2.

Auteurs : Marie-Pierre Péli-Gulli [Suisse] ; Alessandro Sardu [Suisse] ; Nicolas Panchaud [Suisse] ; Serena Raucci [Suisse] ; Claudio De Virgilio [Suisse]

Source :

Cell reports [ 2211-1247 ] ; 2015.

RBID : pubmed:26387955

Descripteurs français

English descriptors

KwdEn :
- Amino Acids (metabolism), Amino Acids (pharmacology), Binding Sites (MeSH), Gene Expression Regulation, Fungal (MeSH), Glutamine (metabolism), Glutamine (pharmacology), Intracellular Membranes (drug effects), Intracellular Membranes (metabolism), Monomeric GTP-Binding Proteins (genetics), Monomeric GTP-Binding Proteins (metabolism), Protein Binding (MeSH), Protein Multimerization (MeSH), Protein Transport (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Transcription Factors (genetics), Transcription Factors (metabolism), Vacuoles (drug effects), Vacuoles (metabolism), Vesicular Transport Proteins (genetics), Vesicular Transport Proteins (metabolism).
MESH :
- chemical , genetics : Monomeric GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Vesicular Transport Proteins.
- chemical , metabolism : Amino Acids, Glutamine, Monomeric GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Vesicular Transport Proteins.
- chemical , pharmacology : Amino Acids, Glutamine.
- drug effects : Intracellular Membranes, Saccharomyces cerevisiae, Vacuoles.
- genetics : Saccharomyces cerevisiae.
- metabolism : Intracellular Membranes, Saccharomyces cerevisiae, Vacuoles.
- Binding Sites, Gene Expression Regulation, Fungal, Protein Binding, Protein Multimerization, Protein Transport, Signal Transduction.

Abstract

Rag GTPases assemble into heterodimeric complexes consisting of RagA or RagB and RagC or RagD in higher eukaryotes, or Gtr1 and Gtr2 in yeast, to relay amino acid signals toward the growth-regulating target of rapamycin complex 1 (TORC1). The TORC1-stimulating state of Rag GTPase heterodimers, containing GTP- and GDP-loaded RagA/B/Gtr1 and RagC/D/Gtr2, respectively, is maintained in part by the FNIP-Folliculin RagC/D GAP complex in mammalian cells. Here, we report the existence of a similar Lst4-Lst7 complex in yeast that functions as a GAP for Gtr2 and that clusters at the vacuolar membrane in amino acid-starved cells. Refeeding of amino acids, such as glutamine, stimulated the Lst4-Lst7 complex to transiently bind and act on Gtr2, thereby entailing TORC1 activation and Lst4-Lst7 dispersal from the vacuolar membrane. Given the remarkable functional conservation of the RagC/D/Gtr2 GAP complexes, our findings could be relevant for understanding the glutamine addiction of mTORC1-dependent cancers.

DOI: 10.1016/j.celrep.2015.08.059
PubMed: 26387955

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Amino Acids (pharmacology)</term>
<term>Binding Sites (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Glutamine (metabolism)</term>
<term>Glutamine (pharmacology)</term>
<term>Intracellular Membranes (drug effects)</term>
<term>Intracellular Membranes (metabolism)</term>
<term>Monomeric GTP-Binding Proteins (genetics)</term>
<term>Monomeric GTP-Binding Proteins (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Protein Transport (MeSH)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
<term>Vacuoles (drug effects)</term>
<term>Vacuoles (metabolism)</term>
<term>Vesicular Transport Proteins (genetics)</term>
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<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Glutamine (métabolisme)</term>
<term>Glutamine (pharmacologie)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Membranes intracellulaires (effets des médicaments et des substances chimiques)</term>
<term>Membranes intracellulaires (métabolisme)</term>
<term>Multimérisation de protéines (MeSH)</term>
<term>Protéines G monomériques (génétique)</term>
<term>Protéines G monomériques (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
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<term>Protéines du transport vésiculaire (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transport des protéines (MeSH)</term>
<term>Vacuoles (effets des médicaments et des substances chimiques)</term>
<term>Vacuoles (métabolisme)</term>
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<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
<term>Vesicular Transport Proteins</term>
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<term>Glutamine</term>
<term>Monomeric GTP-Binding Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
<term>Vesicular Transport Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Amino Acids</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de transcription</term>
<term>Protéines G monomériques</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du transport vésiculaire</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Membranes</term>
<term>Saccharomyces cerevisiae</term>
<term>Vacuoles</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term>
<term>Facteurs de transcription</term>
<term>Glutamine</term>
<term>Membranes intracellulaires</term>
<term>Protéines G monomériques</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du transport vésiculaire</term>
<term>Saccharomyces cerevisiae</term>
<term>Vacuoles</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acides aminés</term>
<term>Glutamine</term>
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<term>Gene Expression Regulation, Fungal</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
<term>Protein Transport</term>
<term>Signal Transduction</term>
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<term>Multimérisation de protéines</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Sites de fixation</term>
<term>Transduction du signal</term>
<term>Transport des protéines</term>
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<front><div type="abstract" xml:lang="en">Rag GTPases assemble into heterodimeric complexes consisting of RagA or RagB and RagC or RagD in higher eukaryotes, or Gtr1 and Gtr2 in yeast, to relay amino acid signals toward the growth-regulating target of rapamycin complex 1 (TORC1). The TORC1-stimulating state of Rag GTPase heterodimers, containing GTP- and GDP-loaded RagA/B/Gtr1 and RagC/D/Gtr2, respectively, is maintained in part by the FNIP-Folliculin RagC/D GAP complex in mammalian cells. Here, we report the existence of a similar Lst4-Lst7 complex in yeast that functions as a GAP for Gtr2 and that clusters at the vacuolar membrane in amino acid-starved cells. Refeeding of amino acids, such as glutamine, stimulated the Lst4-Lst7 complex to transiently bind and act on Gtr2, thereby entailing TORC1 activation and Lst4-Lst7 dispersal from the vacuolar membrane. Given the remarkable functional conservation of the RagC/D/Gtr2 GAP complexes, our findings could be relevant for understanding the glutamine addiction of mTORC1-dependent cancers. </div>
</front>
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<Abstract><AbstractText>Rag GTPases assemble into heterodimeric complexes consisting of RagA or RagB and RagC or RagD in higher eukaryotes, or Gtr1 and Gtr2 in yeast, to relay amino acid signals toward the growth-regulating target of rapamycin complex 1 (TORC1). The TORC1-stimulating state of Rag GTPase heterodimers, containing GTP- and GDP-loaded RagA/B/Gtr1 and RagC/D/Gtr2, respectively, is maintained in part by the FNIP-Folliculin RagC/D GAP complex in mammalian cells. Here, we report the existence of a similar Lst4-Lst7 complex in yeast that functions as a GAP for Gtr2 and that clusters at the vacuolar membrane in amino acid-starved cells. Refeeding of amino acids, such as glutamine, stimulated the Lst4-Lst7 complex to transiently bind and act on Gtr2, thereby entailing TORC1 activation and Lst4-Lst7 dispersal from the vacuolar membrane. Given the remarkable functional conservation of the RagC/D/Gtr2 GAP complexes, our findings could be relevant for understanding the glutamine addiction of mTORC1-dependent cancers. </AbstractText>
<CopyrightInformation>Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.</CopyrightInformation>
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<Author ValidYN="Y"><LastName>Raucci</LastName>
<ForeName>Serena</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>De Virgilio</LastName>
<ForeName>Claudio</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland. Electronic address: claudio.devirgilio@unifr.ch.</Affiliation>
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<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
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<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
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<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
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<MeshHeading><DescriptorName UI="D014617" MajorTopicYN="N">Vacuoles</DescriptorName>
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<MeshHeading><DescriptorName UI="D033921" MajorTopicYN="N">Vesicular Transport Proteins</DescriptorName>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year>
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<Day>07</Day>
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<PubMedPubDate PubStatus="revised"><Year>2015</Year>
<Month>07</Month>
<Day>21</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>08</Month>
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<ArticleId IdType="doi">10.1016/j.celrep.2015.08.059</ArticleId>
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<affiliations><list><country><li>Suisse</li>
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<region><li>Canton de Fribourg</li>
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<orgName><li>Université de Fribourg</li>
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<tree><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Peli Gulli, Marie Pierre" sort="Peli Gulli, Marie Pierre" uniqKey="Peli Gulli M" first="Marie-Pierre" last="Péli-Gulli">Marie-Pierre Péli-Gulli</name>
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<name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name>
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</record>

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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2.

Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2.

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